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Q27772 (C1TC_SPOFR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-1-tetrahydrofolate synthase, cytoplasmic

Short name=C1-THF synthase

Including the following 3 domains:

  1. Methylenetetrahydrofolate dehydrogenase
    EC=1.5.1.5
  2. Methenyltetrahydrofolate cyclohydrolase
    EC=3.5.4.9
  3. Formyltetrahydrofolate synthetase
    EC=6.3.4.3
OrganismSpodoptera frugiperda (Fall armyworm)
Taxonomic identifier7108 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeAmphipyrinaeSpodoptera

Protein attributes

Sequence length933 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP-Rule MF_01543

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01543

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01543

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01543.

Domain

This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity. HAMAP-Rule MF_01543

Sequence similarities

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 933933C-1-tetrahydrofolate synthase, cytoplasmic HAMAP-Rule MF_01543
PRO_0000199325

Regions

Nucleotide binding170 – 1723NADP By similarity
Nucleotide binding378 – 3858ATP By similarity
Region1 – 303303Methylenetetrahydrofolate dehydrogenase and cyclohydrolase HAMAP-Rule MF_01543
Region51 – 555Substrate binding By similarity
Region98 – 1003Substrate binding By similarity
Region270 – 2745Substrate binding By similarity
Region304 – 933630Formyltetrahydrofolate synthetase HAMAP-Rule MF_01543

Sites

Binding site1951NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q27772 [UniParc].

Last modified January 16, 2004. Version 3.
Checksum: 55C3FA820C1A55CB

FASTA933100,618
        10         20         30         40         50         60 
MWEPQGSLDP VLESIENELR DQVAEARSRW AGFDARLAIV QVGGREDSNV YIRMKLRAAE 

        70         80         90        100        110        120 
NIGITAEHIQ LPRDITETEL LANITSLNES PYVHGIIVQM PLDSVHPIDS HAITDAVSPD 

       130        140        150        160        170        180 
KDVDGLNTIN EGRVRVGDLS GFIPCTPAGC VELIKRTGVT IAGKNVVVLG RSRIVGTPVS 

       190        200        210        220        230        240 
ELLKWEHATV TVCHSKTKNL SEITKTADIL VVAIGRGEMV RGSWIKPGAV VIDCGINPIS 

       250        260        270        280        290        300 
DPTKKSGQRL VGDVAYEEAV QVASHVTPVP GGVGPMTVAM LMRNTVQAAR RQLDRLLAPT 

       310        320        330        340        350        360 
WPLRPLRITP LSPPPSDIVI ARSQKPKDIS ELAHEIGLFS NEVSQYGRTK AKISLSVLDR 

       370        380        390        400        410        420 
MRNQQGAKYI VVAGITPTPL GEGKSTTLLG LVQALSAHRG RNSFAVMRQP SQGPTFGVKG 

       430        440        450        460        470        480 
GAAGGGYSQV IPMEEFNLHL TGDIHAGTAA NNLLAAQMDA RIFHELTQKD GPLFDRLVPK 

       490        500        510        520        530        540 
IKGVRKFSPI QLRRLKRLGI TKTDPDTLTE GEKSKFARLN IDTSKIMWNR VVDLNDRYLR 

       550        560        570        580        590        600 
KITVGQSPTE KGFTRETAFD ISVASEIMAI LALGRDVEDI KERLANMVVA LDKSGNPVTA 

       610        620        630        640        650        660 
DDLGMTGALL VLLRDAFEPT LMQSLEGTPV LVHTGPFANI RHGCSSILAD KIAMKLAGEN 

       670        680        690        700        710        720 
GYVATEAGFG SDIGMEKFFD IKCRASGDTP HCAVIVSTVR ALKMHGGGPP VSAGMPLNDV 

       730        740        750        760        770        780 
YVQENLELLS KGLCNLGKHI SNGNKFGVPV VVAINKHGND TPAELNLVKE FAVKNGAFRA 

       790        800        810        820        830        840 
VLCDHWAKGG LGALELADAV IEACDSKSKF DFLYPLQLSI QEKIQIIAKE MYGAGQVEYT 

       850        860        870        880        890        900 
DEVLEKIKTF TDMGYDKFPI CMAKTSNSLT GDPAVKGAPT GFTLKINGIF ASVGAGFVVP 

       910        920        930 
MVGEISKMPG LPTRPSIYDI DLNTKTGEIE GLF 

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References

[1]"Primary structure of a folate-dependent trifunctional enzyme from Spodoptera frugiperda."
Tremblay G.B., MacKenzie R.E.
Biochim. Biophys. Acta 1261:129-133(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L36189 mRNA. Translation: AAA74302.1.
PIRS53523.

3D structure databases

ProteinModelPortalQ27772.
SMRQ27772. Positions 10-294, 467-528.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00193.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSPR00085. THFDHDRGNASE.
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC1TC_SPOFR
AccessionPrimary (citable) accession number: Q27772
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: April 16, 2014
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways